Purification, crystallization and preliminary crystallographic characterization of the α2,6-sialyltransferase from Photobacterium sp. JT-ISH-224

Nozomu Okino, Yoshimitsu Kakuta, Hitomi Kajiwara, Masako Ichikawa, Yoshimitsu Takakura, Makoto Ito, Takeshi Yamamoto

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

Sialyltransferases transfer sialic acid from cytidine-5-monophospho-N- acetylneuraminic acid (CMP-NeuAc) to the nonreducing termini of the oligosaccharyl structures of various glycoproteins and glycolipids. The newly cloned α2,6-sialyltransferase from Photobacterium sp. JT-ISH-224 (from the Vibrionaceae family) is composed of two domains: an unknown N-terminal domain and a catalytic C-terminal domain which shares significant homology with the Pasteurella multocida multifunctional sialyltransferase. The putative mature form of JT-ISH-224 α2,6-sialyltransferase was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystal belonged to space group P3121 or P3 221, with unit-cell parameters a = b = 90.29, c = 204.33 Å. X-ray diffraction data were collected to 2.5 Å resolution.

Original languageEnglish
Pages (from-to)662-664
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number8
DOIs
Publication statusPublished - Jul 28 2007

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Fingerprint Dive into the research topics of 'Purification, crystallization and preliminary crystallographic characterization of the α2,6-sialyltransferase from Photobacterium sp. JT-ISH-224'. Together they form a unique fingerprint.

Cite this